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Published in 2018 at "Planta medica"
DOI: 10.1055/a-0635-8369
Abstract: Plants are sessile organisms. Therefore, they developed the capacity to quickly respond to biotic and abiotic environmental stresses, for instance by producing a broad spectrum of bioactive specialized metabolites. In this defense response, the jasmonate…
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Keywords:
endoplasmic reticulum;
metabolism;
degradation erad;
reticulum associated ... See more keywords
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Published in 2019 at "Critical Reviews in Biochemistry and Molecular Biology"
DOI: 10.1080/10409238.2019.1610351
Abstract: Abstract About 40% of the eukaryotic cell’s proteins are inserted co- or post-translationally in the endoplasmic reticulum (ER), where they attain the native structure under the assistance of resident molecular chaperones and folding enzymes. Subsequently,…
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Keywords:
degradation;
degradation erad;
clearance;
degradation erlad ... See more keywords
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Published in 2022 at "Cold Spring Harbor perspectives in biology"
DOI: 10.1101/cshperspect.a041247
Abstract: Misfolded, potentially toxic proteins in the lumen and membrane of the endoplasmic reticulum (ER) are eliminated by proteasomes in the cytosol through ER-associated degradation (ERAD). The ERAD process involves the recognition of substrates in the…
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Keywords:
endoplasmic reticulum;
degradation erad;
reticulum associated;
protein degradation ... See more keywords
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Published in 2017 at "Journal of Cell Science"
DOI: 10.1242/jcs.206847
Abstract: ABSTRACT The mammalian ubiquitin ligase Hrd1 is the central component of a complex facilitating degradation of misfolded proteins during the ubiquitin–proteasome-dependent process of ER-associated degradation (ERAD). Hrd1 associates with cofactors to execute ERAD, but their…
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Keywords:
degradation;
degradation erad;
hrd1;
ubiquitin ligase ... See more keywords